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Protein

Polyketide synthase BAS

Gene

BAS

Organism
Rheum palmatum (Chinese rhubarb)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Polyketide synthase producing 4-hydroxybenzalacetone. Can use p-coumaryl-CoA as substrate but does not accept hexanoyl-CoA, isobutyryl-CoA, isovaleryl-CoA, and acetyl-CoA as a substrates. Catalyzes the initial key reaction step in the biosynthesis of phenylbutanoids.2 Publications

Catalytic activityi

4-coumaroyl-CoA + malonyl-CoA + H2O = 2 CoA + 4-hydroxybenzalacetone + 2 CO2.2 Publications

Kineticsi

kcat is 1.79 min(-1) with 4-coumaroyl-CoA as substrate (at pH 8 and 30 degrees Celsius).

  1. KM=10 µM for 4-coumaroyl-CoA (at pH 8 and 30 degrees Celsius)2 Publications

    pH dependencei

    Optimum pH is 8.0-8.8.2 Publications

    Pathwayi: flavonoid biosynthesis

    This protein is involved in the pathway flavonoid biosynthesis, which is part of Secondary metabolite biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway flavonoid biosynthesis and in Secondary metabolite biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei157 – 1571Nucleophile and monoketide coumarate intermediate1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Ligandi

    Chromophore

    Enzyme and pathway databases

    BRENDAi2.3.1.212. 13067.
    UniPathwayiUPA00154.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polyketide synthase BAS (EC:2.3.1.212)
    Alternative name(s):
    Benzalacetone synthase
    Short name:
    RpBAS
    Gene namesi
    Name:BAS
    OrganismiRheum palmatum (Chinese rhubarb)
    Taxonomic identifieri137221 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesPolygonaceaePolygonoideaeRumiceaeRheum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi190 – 1901C → G or T: Normal benzalacetone synthase activity. 1 Publication
    Mutagenesisi207 – 2082IL → LF: Acquires an additional chalcone synthase activity. 1 Publication
    Mutagenesisi249 – 2491G → L: Reduced benzalacetone synthase activity. 1 Publication
    Mutagenesisi331 – 3311S → V: Enhanced benzalacetone synthase activity. 1 Publication

    Chemistry

    ChEMBLiCHEMBL1075247.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 384384Polyketide synthase BASPRO_0000424291Add
    BLAST

    Keywords - PTMi

    Hydroxylation

    Interactioni

    Subunit structurei

    Homodimer.

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    DIPiDIP-58521N.

    Structurei

    Secondary structure

    1
    384
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 189Combined sources
    Beta strandi23 – 253Combined sources
    Turni26 – 283Combined sources
    Helixi29 – 368Combined sources
    Helixi43 – 5412Combined sources
    Turni55 – 573Combined sources
    Beta strandi60 – 623Combined sources
    Helixi67 – 726Combined sources
    Helixi74 – 774Combined sources
    Beta strandi78 – 825Combined sources
    Helixi84 – 11027Combined sources
    Helixi114 – 1163Combined sources
    Beta strandi119 – 1268Combined sources
    Beta strandi129 – 1313Combined sources
    Helixi133 – 1408Combined sources
    Beta strandi148 – 1547Combined sources
    Helixi159 – 17315Combined sources
    Beta strandi178 – 1858Combined sources
    Turni188 – 1903Combined sources
    Helixi204 – 2074Combined sources
    Beta strandi211 – 22010Combined sources
    Turni223 – 2253Combined sources
    Beta strandi230 – 23910Combined sources
    Beta strandi246 – 2527Combined sources
    Beta strandi255 – 2606Combined sources
    Helixi264 – 28017Combined sources
    Helixi281 – 2833Combined sources
    Helixi288 – 2903Combined sources
    Beta strandi291 – 2955Combined sources
    Helixi300 – 31011Combined sources
    Helixi314 – 3174Combined sources
    Helixi318 – 32710Combined sources
    Helixi331 – 3333Combined sources
    Helixi334 – 34815Combined sources
    Turni354 – 3574Combined sources
    Beta strandi359 – 3679Combined sources
    Turni368 – 3703Combined sources
    Beta strandi371 – 3799Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3A5QX-ray1.80A/B1-384[»]
    3A5RX-ray1.60A/B1-384[»]
    3A5SX-ray1.80A/B1-384[»]
    ProteinModelPortaliQ94FV7.
    SMRiQ94FV7. Positions 10-382.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ94FV7.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the chalcone/stilbene synthases family.Curated

    Family and domain databases

    Gene3Di3.40.47.10. 2 hits.
    InterProiIPR012328. Chalcone/stilbene_synth_C.
    IPR001099. Chalcone/stilbene_synthase_N.
    IPR011141. Polyketide_synthase_type-III.
    IPR016039. Thiolase-like.
    [Graphical view]
    PfamiPF02797. Chal_sti_synt_C. 1 hit.
    PF00195. Chal_sti_synt_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000451. PKS_III. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q94FV7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MATEEMKKLA TVMAIGTANP PNCYYQADFP DFYFRVTNSD HLINLKQKFK
    60 70 80 90 100
    RLCENSRIEK RYLHVTEEIL KENPNIAAYE ATSLNVRHKM QVKGVAELGK
    110 120 130 140 150
    EAALKAIKEW GQPKSKITHL IVCCLAGVDM PGADYQLTKL LDLDPSVKRF
    160 170 180 190 200
    MFYHLGCYAG GTVLRLAKDI AENNKGARVL IVCSEMTTTC FRGPSETHLD
    210 220 230 240 250
    SMIGQAILGD GAAAVIVGAD PDLTVERPIF ELVSTAQTIV PESHGAIEGH
    260 270 280 290 300
    LLESGLSFHL YKTVPTLISN NIKTCLSDAF TPLNISDWNS LFWIAHPGGP
    310 320 330 340 350
    AILDQVTAKV GLEKEKLKVT RQVLKDYGNM SSATVFFIMD EMRKKSLENG
    360 370 380
    QATTGEGLEW GVLFGFGPGI TVETVVLRSV PVIS
    Length:384
    Mass (Da):42,225
    Last modified:December 1, 2001 - v1
    Checksum:i4068107D7A3EE4B0
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF326911 mRNA. Translation: AAK82824.1.

    Genome annotation databases

    KEGGiag:AAK82824.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF326911 mRNA. Translation: AAK82824.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3A5QX-ray1.80A/B1-384[»]
    3A5RX-ray1.60A/B1-384[»]
    3A5SX-ray1.80A/B1-384[»]
    ProteinModelPortaliQ94FV7.
    SMRiQ94FV7. Positions 10-382.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-58521N.

    Chemistry

    ChEMBLiCHEMBL1075247.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAK82824.

    Enzyme and pathway databases

    UniPathwayiUPA00154.
    BRENDAi2.3.1.212. 13067.

    Miscellaneous databases

    EvolutionaryTraceiQ94FV7.

    Family and domain databases

    Gene3Di3.40.47.10. 2 hits.
    InterProiIPR012328. Chalcone/stilbene_synth_C.
    IPR001099. Chalcone/stilbene_synthase_N.
    IPR011141. Polyketide_synthase_type-III.
    IPR016039. Thiolase-like.
    [Graphical view]
    PfamiPF02797. Chal_sti_synt_C. 1 hit.
    PF00195. Chal_sti_synt_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000451. PKS_III. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.
    ProtoNetiSearch...

    Publicationsi

    1. "Benzalacetone synthase. A novel polyketide synthase that plays a crucial role in the biosynthesis of phenylbutanones in Rheum palmatum."
      Abe I., Takahashi Y., Morita H., Noguchi H.
      Eur. J. Biochem. 268:3354-3359(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, HOMODIMER, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY.
      Tissue: Leaf.
    2. "Structure function analysis of benzalacetone synthase from Rheum palmatum."
      Abe T., Morita H., Noma H., Kohno T., Noguchi H., Abe I.
      Bioorg. Med. Chem. Lett. 17:3161-3166(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-190; GLY-249 AND SER-331, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    3. "A structure-based mechanism for benzalacetone synthase from Rheum palmatum."
      Morita H., Shimokawa Y., Tanio M., Kato R., Noguchi H., Sugio S., Kohno T., Abe I.
      Proc. Natl. Acad. Sci. U.S.A. 107:669-673(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), S-(4-HYDROXYCINNAMYL)CYSTEINE AT CYS-157, HOMODIMER, MUTAGENESIS OF 207-ILE-LEU-208, ACTIVE SITE.

    Entry informationi

    Entry nameiBAS_RHEPA
    AccessioniPrimary (citable) accession number: Q94FV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2013
    Last sequence update: December 1, 2001
    Last modified: April 13, 2016
    This is version 61 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.